Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface

Article Abstract:

A structural analysis of the guanine-nucleotide-exchange factor human Mss4 (hMss4) using multidimensional nuclear magnetic resonance reveals that Mss4 is a protein consisting of a central seven-stranded antiparallel beta-sheet between two small sheets, one a three-stranded and the other a beta hairpin. hMss4 binding to Sec 4 appears to involve the Zn2+-binding region and the GH adjacent loop which are also responsible fore hMss4's GEF activity. The common recognition of Ras proteins between hMss4 and other guanine-nucleotide-exchange factors suggests the presence of common structural elements even though their sequences are very different.

Usage, Nuclear magnetic resonance

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Crystal structure of a DExx box DNA helicase

Article Abstract:

The crystal structure of a monomeric form of a DNA helicase from Bacillus stearothermophilus shows the presence of two domains with a deep gap between them. The ATP-binding site is situated at the bottom of the cleft. The site is the result of the motifs preserved across the group of associated helicases. The ATP-binding site also has a structural homology with RecA. RecA is the DNA recombination protein. This shows that hydrolysis and ATP binding may lead to changes in the enzyme during the process of catalysis. This indicates the presence of a common mechanism in all helicases.

Analysis, DNA, Enzymes, Adenosine triphosphate, ATP, Enzyme structure-activity relationships

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Crystal structure of a streptococcal protein G domain bound to an Fab fragment

Article Abstract:

A Streptococcus cell-surface protein, called protein G, has a high affinity for the Fab part of immunoglobulin (IgG), and this has consequences for molecular recognition. The crystal structure of a complex between an immunoglobulin Fab fragment and a protein G domain is described and illustrated. The structure ingeniously facilitates the maintenance of a high affinity for many different IgG molecules. It also sheds light on the interaction of Fab's constant regions with another protein.

Streptococcus, Immunoglobulins, Immune recognition

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